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Is the heme pocket region modulated by disulfide-bridge formation in fish and amphibian neuroglobins as in humans?
- Source :
- Biochimica et biophysica acta : proteins and proteomics
- Publication Year :
- 2013
- Publisher :
- Elsevier BV, 2013.
-
Abstract
- Neuroglobin, a globin characterized by a bis-histidine ligation of the heme iron, has been identified in mammalian and non-mammalian vertebrates, including fish, amphibians and reptiles. In human neuroglobin, the presence of an internal disulfide bond in the CD loop (CD7–D5) is found to modulate the ligand binding through a change in the heme pocket structure. Although the neuroglobin sequences mostly display conserved Cys at positions CD7, D5 and G18/19, a number of exceptions are known. In this study, neuroglobins from amphibian (Xenopus tropicalis) and fish (Chaenocephalus aceratus, Dissostichus mawsoni and Danio rerio) are investigated using electron paramagnetic resonance and optical absorption spectroscopy. All these neuroglobins differ from human neuroglobin in their Cys-positions. It is demonstrated that if disulfide bonds are formed in fish and amphibian neuroglobins, the reduction of these bonds does not result in alteration of the heme pocket in these globins. Furthermore, it is shown that mutagenesis of the Cys residues of X. tropicalis neuroglobin influences the protein structure. The amphibian neuroglobin is also found to be more resistant to H2O2-induced denaturation than the other neuroglobins under study, although all show an overall large stability in high concentrations of this oxidant. This article is part of a Special Issue entitled: Oxygen Binding and Sensing Proteins.
- Subjects :
- Protein Folding
Hemeprotein
Xenopus
Molecular Sequence Data
Biophysics
Neuroglobin
Nerve Tissue Proteins
Heme
Biochemistry
Analytical Chemistry
chemistry.chemical_compound
Protein structure
Animals
Humans
Denaturation (biochemistry)
Amino Acid Sequence
Cysteine
Disulfides
Globin
Biology
Molecular Biology
Sequence Homology, Amino Acid
biology
Physics
Electron Spin Resonance Spectroscopy
Fishes
Hydrogen Peroxide
biology.organism_classification
Globins
Chemistry
chemistry
Human medicine
Oxygen binding
Protein Binding
Subjects
Details
- ISSN :
- 15709639
- Volume :
- 1834
- Database :
- OpenAIRE
- Journal :
- Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
- Accession number :
- edsair.doi.dedup.....b6f44388b8e7211e243540870e88b5f9